82 kDa matrix metalloproteinase-9, 92 kDa gelatinase, 92 kDa type IV collagenase, CLG 4B, CLG4B, Collagenase Type 4 beta, Collagenase type IV 92 KD, EC 3.4.24.35, Gelatinase 92 KD, Gelatinase B, Gelatinase beta, GelatinaseB, GELB, Macrophage gelatinase, MANDP2, Matrix metallopeptidase 9 (gelatinase
The matrix metalloproteinases (MMP) are a family of peptidase enzymes responsible for the degradation of extracellular matrix components, including collagen, gelatin, fibronectin, laminin and proteoglycan. Transcription of MMP genes is differentially activated by phorbol ester, lipopolysaccharide (LPS) or staphylococcal enterotoxin B (SEB). MMP catalysis requires both calcium and zinc. MMP-9 (also designated 92 kDa type IV collagenase or gelatinase B) has been shown to degrade bone collagens in concert with MMP-1 (also designated interstitial collagenase, fibroblast collagenase or collagenase-1), and cysteine proteases and may play a role in bone osteoclastic resorption. MMP-1 is down-regulated by p53, and abnormality of p53 expression may contribute to joint degradation in rheumatoid arthritis by regulating MMP-1 expression.
Immunohistochemistry (Formalin-fixed) (1-2µg/ml for 30 minutes at RT)(Staining of formalin-fixed tissues requires heating tissue sections in 10mM Tris with 1mM EDTA, pH 9.0, for 45 min at 95&degC followed by cooling at RT for 20 minutes),
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